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Y.H., Ding, S.T., Chang, M.H., 2006. Effect of fumonisins on macrophage immune functions and gene expression of cytokines in broilers. Arch. Anim. Nutr. 60 (4), 267-276. 950 Oka, H., Emori, Y., Kobayashi, N., Hayashi, Y., Nomoto, K., 2001. Suppression of allergic reactions by royal jelly in association with the restoration of macrophage function and the improvement of Th1/Th2 cell responses. Int. Immunopharmacol. 1, 521-532. 951 Kataoka, M., Arai, N., Taniguchi, Y., Kohno, K., Iwaki, K., Ikeda, M., Kurimoto, M.
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of cytokines in broilers. Arch. Anim. Nutr. 60 (4), 267-276. 950 Oka, H., Emori, Y., Kobayashi, N., Hayashi, Y., Nomoto, K., 2001. Suppression of allergic reactions by royal jelly in association with the restoration of macrophage function and the improvement of Th1/Th2 cell responses. Int. Immunopharmacol. 1, 521-532. 951 Kataoka, M., Arai, N., Taniguchi, Y., Kohno, K., Iwaki, K., Ikeda, M., Kurimoto, M., 2001. Analysis of anti allergic function of royal jelly. Natural Med. 55, 174-180. 952 Townsend, G.F., Morgan
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association with the restoration of macrophage function and the improvement of Th1/Th2 cell responses. Int. Immunopharmacol. 1, 521-532. 951 Kataoka, M., Arai, N., Taniguchi, Y., Kohno, K., Iwaki, K., Ikeda, M., Kurimoto, M., 2001. Analysis of anti allergic function of royal jelly. Natural Med. 55, 174-180. 952 Townsend, G.F., Morgan, J.F., Hazlett, B., 1959. Activity of 10 hydroxydecenoic acid from royal jelly against experimental leukemia and ascitic tumors. Nature 183, 1270- 1271. 953 Townsend, G.F., Morgan, J.F., Tolnai, S., Hazlett
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vitro antitumor activity of fatty acid I. 10-Hydroxy-2-decenoic acid from royal jelly. Cancer Res. 20, 503-510. 954 Townsend, G.F., Brown, W.H., Felauer, E.E., Hazlett, B., 1961. Studies on the in vitro antitumor activity of fatty acid IV. The esters of acids closely related to 10-hydroxy-2 MICROGRAFII ASUPRA PRODUSELOR APICOLE Andrițoiu Călin Vasile 233 2001955; Koya Miyata et al, 2004956; Mishima et al, 2005957; Fujii et al, 1990958; Kohno et al., 2004959). Efectul antioxidant al lăptișorului de matcă (LM) Deși unele
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activității biologice. Proteinele sunt componentele principale ale LM și constituie aproximativ jumătate din decenoic acid from royal jelly against transplantable mouse leukaemia. Can. J. Biochem. Physiol. 39, 1765-1770. 955 Kamakura, M., Mitani, N., Fukuda, T., Fukushima, M., 2001. Antifatigue effect of fresh royal jelly in mice. J. Nutr. Sci. Vitaminol. 47, 394-401. 956 Koya-Miyata, S., Okamoto, I., Ushio, S., Iwaki, K., Ikeda, M., Kurimoto, M., 2004. Identification of a collagen production promoting factor from an extract of royal jelly and its
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M., 2001. Antifatigue effect of fresh royal jelly in mice. J. Nutr. Sci. Vitaminol. 47, 394-401. 956 Koya-Miyata, S., Okamoto, I., Ushio, S., Iwaki, K., Ikeda, M., Kurimoto, M., 2004. Identification of a collagen production promoting factor from an extract of royal jelly and its possible mechanism. Biosci. Biotechnol. Biochem. 68, 767-773. 957 Mishima, S., Suzuki, K., Isohama, Y., Kuratsu, N., Araki, Y., Inoue, M., Miyata, T., 2005. Royal jelly has estrogenic effects in vitro and in vivo. J. Ethnopharmacol. 101
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Iwaki K, Ikeda M, et al. Major royal jelly protein 3 modulates immune responses in vitro and in vivo. Life Sci 2003;73: 2029- 45. 963 Šimúth J, Bíliková K, Kováčová E, Kuzmová Z, Schroder W. Immunochemical approach to detection of adulteration in honey: physiologically active royal jelly protein stimulating TNF-a is a regular component of honey. J Agric Food Chem 2004;52:2154-8. MICROGRAFII ASUPRA PRODUSELOR APICOLE 234 materia uscată (Tomoda et al, 1977964; Takenaka, 1982965; Howe et al
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and in vivo. Life Sci 2003;73: 2029- 45. 963 Šimúth J, Bíliková K, Kováčová E, Kuzmová Z, Schroder W. Immunochemical approach to detection of adulteration in honey: physiologically active royal jelly protein stimulating TNF-a is a regular component of honey. J Agric Food Chem 2004;52:2154-8. MICROGRAFII ASUPRA PRODUSELOR APICOLE 234 materia uscată (Tomoda et al, 1977964; Takenaka, 1982965; Howe et al, 1985966; Schmitzova et al, 1998967), identitatea acestora fiind parțial cunoscută (Fujiwara et al, 1990968; Hanes și
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Nagai & 964 Tomoda, G., Matsuyama, J., Matsuka, M., 1977. Studies on protein in royal jelly 2. Fractionation of water-soluble protein by DEAEcellulose chromatography, gel filtration and disc electrophoresis. Journal of Apicultural Research 16, 123-130. 965 Takenaka, T., 1982. Chemical composition of royal jelly. Honeybee Science 3, 69-74. 966 Howe, S.R., Dimick, P.S., Benton, A.W., 1985. Composition of freshly harvested and commercial royal jelly. Journal of Apicultural Research 24, 52-61. 967 Schmitzová, J., Klaudiny, J., Albert, Š, Schröder, W., Schreckengost, W
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Dimick, P.S., Benton, A.W., 1985. Composition of freshly harvested and commercial royal jelly. Journal of Apicultural Research 24, 52-61. 967 Schmitzová, J., Klaudiny, J., Albert, Š, Schröder, W., Schreckengost, W., Hanes, J., Júdová, J., Šimúth, J., 1998. A family of major royal jelly proteins of the honey bee Apis mellifera L. Cellular and Molecular Life Sciences 54, 1020-1030. 968 Fujiwara, S., Imai, J., Fujiwara, M., Yaeshima, T., Kawashima, T., Kobayashi, K., 1990. A potent antibacterial protein in royal jelly. Purification
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L). Journal of Apicultural Research 31, 22- 26. 970 Klaudiny, J., Hanes, J., Kulifajova, J., Alberts, Š, Šimuth, J., 1994. Molecular cloning of two cDNAs from the head of the nurse honey bee (Apis mellifera L.) for coding related proteins of royal jelly. Journal of Apicultural Research 33, 105-111. 971 Watanabe, K., Shinmoto, H., Kobori, M., Tsushida, T., Shinohara, K., Kanaeda, J., Yonekura, M., 1998. Stimulation of cell growth in the U-927 human myeloid cell line by honey royal jelly protein
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K., Kanaeda, J., Yonekura, M., 1998. Stimulation of cell growth in the U-927 human myeloid cell line by honey royal jelly protein. Cytotechnology 26, 23-27. 972 Albert, Š., Klaudiny, J., Šimúth, J., 1999. Molecular characterization of MRJP3, highly polymorphic protein of honeybee (Apis mellifera) royal jelly. Insect Biochemistry and Molecular Biology 29, 427-434. 973 Tomoda, G., Matsuyama, J., Matsuka, M., 1977. Studies on protein in royal jelly 2. Fractionation of water soluble protein by DEAEcellulose chromatography, gel filtration and disc electrophoresis
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Chen, S., 1995. Changes in protein components and storage stability of royal jelly under various conditions. Food Chemistry 54, 195-200. 976 Schmitzová, J., Klaudiny, J., Albert, Š., Schröder, W., Schreckengost, W., Hanes, J., Júdová, J., Šimúth, J., 1998. A family of major royal jelly proteins of the honey bee Apis mellifera L. Cellular and Molecular Life Sciences 54, 1020- 1030. MICROGRAFII ASUPRA PRODUSELOR APICOLE Andrițoiu Călin Vasile 235 Inoue, 2004977) iar hidrolizat cu protează N arată cea mai mare activitate antioxidantă
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hipofaringeale ale albinei adulte (Kucharski et al., 1998985; Hanes et Šimúth, 1992986; Kubo et al., 1996987). Apa1 este o glicoproteină cu o masă moleculara de 55 kDa (Schmitzová et 977 Nagai, T., & Inoue, R. (2004). Preparation and the functional properties of water extract and alkaline extract from royal jelly. Food Chemistry, 84, 181-186. 978 Guo, H., Kozuma, Y., & Yonekura, M. (2005). Isolation and properties of antioxidative peptides from water-soluble royal jelly protein hydrolysate. Food Science Technology Research, 11, 222-230. 979 Guo
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Guo Hang, Yoshiaki Kouzuma, Masami Yonekura, Structures and properties of antioxidative peptides derived from royal jelly protein, Food Chemistry 113 (2009) 238- 245. 980 Schmitzová J, Klaudiny J, Albert Š, Hanes J, Schroder W, Schrockengost V, et al. A family of major royal jelly proteins of the honeybee Apis mellifera L. Cell Mol Life Sci 1998;54:1020-30. 981 Matui, T., Yukiyoshi, A., Doi, S., Sugimoto, H., Yamada, H., Matsumoto, K., 2002. Gastrointestinal enzyme production of bioactive peptides from royal jelly
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V, et al. A family of major royal jelly proteins of the honeybee Apis mellifera L. Cell Mol Life Sci 1998;54:1020-30. 981 Matui, T., Yukiyoshi, A., Doi, S., Sugimoto, H., Yamada, H., Matsumoto, K., 2002. Gastrointestinal enzyme production of bioactive peptides from royal jelly and their antihypertensive ability in SHR. Journal of Nutrition Biochemistry 13, 80-86. 982 Albert, S., Klaudiny, J., Simuth, J., 1999. Molecular characterization of MRJP3, highly polymorphic protein of honeybee (Apis mellifera) royal jelly. Insect Biochemical
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H., Matsumoto, K., 2002. Gastrointestinal enzyme production of bioactive peptides from royal jelly and their antihypertensive ability in SHR. Journal of Nutrition Biochemistry 13, 80-86. 982 Albert, S., Klaudiny, J., Simuth, J., 1999. Molecular characterization of MRJP3, highly polymorphic protein of honeybee (Apis mellifera) royal jelly. Insect Biochemical and Molecular Biology 29, 427-434. 983 Klaudiny, J., Hanes, J., Kulifajova, J., Albert, S., Simuth, J., 1994. Molecular cloning of two cDNA from the head of the nurse honey bee (Apis mellifera L.
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jelly. Insect Biochemical and Molecular Biology 29, 427-434. 983 Klaudiny, J., Hanes, J., Kulifajova, J., Albert, S., Simuth, J., 1994. Molecular cloning of two cDNA from the head of the nurse honey bee (Apis mellifera L.) coding for related proteins of royal jelly. Journal of Apicultural Research 33, 105-111. 984 Schmitzova, J., Klaudiny, J., Albert, S., Schroder, W., Schreckengost, W., Hanes, J., Judova, J., Simuth, J., 1998. A family of major royal jelly proteins of the honeybee Apis mellifera L. Cellular
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the nurse honey bee (Apis mellifera L.) coding for related proteins of royal jelly. Journal of Apicultural Research 33, 105-111. 984 Schmitzova, J., Klaudiny, J., Albert, S., Schroder, W., Schreckengost, W., Hanes, J., Judova, J., Simuth, J., 1998. A family of major royal jelly proteins of the honeybee Apis mellifera L. Cellular and Molecular Life Sciences 54, 1020-1030. 985 Kucharski R, Maleszka R, Hayward DC, Ball EE. A royal jelly protein is expressed in a subset of Kenyon cells in the
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J., 1998. A family of major royal jelly proteins of the honeybee Apis mellifera L. Cellular and Molecular Life Sciences 54, 1020-1030. 985 Kucharski R, Maleszka R, Hayward DC, Ball EE. A royal jelly protein is expressed in a subset of Kenyon cells in the mushroom bodies of the honeybee brain. Die Naturwissenschaften 1998; 85:343- 6. 986 Hanes J, Šimúth J. Identification and partial characterization of the major royal jelly protein of the honeybee (Apis mellifera L.). J Apic Res
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asupra radicalilor superoxid. LM a demonstrat o activitate maximă fiind depășit doar de propolis. În plus, Nagai și Inoue (2004996) și Nagai et 988 Schmitzová J, Klaudiny J, Albert Š, Hanes J, Schroder W, Schrockengost V, et al. A family of major royal jelly proteins of the honeybee Apis mellifera L. Cell Mol Life Sci 1998;54:1020-30. 989 Hanes J, Šimúth J. Identification and partial characterization of the major royal jelly protein of the honeybee (Apis mellifera L.). J Apic
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enhances proliferation of primary cultured rat hepatocytes and increases albumin production in the absence of serum. Biochem Biophys Res Commun 2001;282:865- 74. 991 Matsui T, Yukiyoshi A, Doi S, Sugimoto H, Yamada H, Matsumoto K. Gastrointestinal enzyme production of bioactive peptides from royal jelly protein and their antihypertensive ability in SHR. J Nutr Biochem 2002;13:80- 6. 992 Fontana R, Mendes MA, Monson de Souza B, Konno K, César LMM, Malaspina O, et al. Jelleines: a family of
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of bioactive peptides from royal jelly protein and their antihypertensive ability in SHR. J Nutr Biochem 2002;13:80- 6. 992 Fontana R, Mendes MA, Monson de Souza B, Konno K, César LMM, Malaspina O, et al. Jelleines: a family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera). Peptides 2004;25:919- 28. 993 Matui, T., Yukiyoshi, A., Doi, S., Sugimoto, H., Yamada, H., Matsumoto, K., 2002. Gastrointestinal enzyme production of bioactive peptides from royal jelly and their
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Malaspina O, et al. Jelleines: a family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera). Peptides 2004;25:919- 28. 993 Matui, T., Yukiyoshi, A., Doi, S., Sugimoto, H., Yamada, H., Matsumoto, K., 2002. Gastrointestinal enzyme production of bioactive peptides from royal jelly and their antihypertensive ability in SHR. Journal of Nutrition Biochemistry 13, 80-86. 994 Aziza A. El-Nekeetya, Wafaa El Kholyb, Naglaa F. Abbasc, Ahmad Ebaidb, Hassan A. Amraa, Mosaad A. Abdel-Wahhaba, Efficacy of royal jelly against
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T., Sakai, M., Inoue, R., Inoue, H., Suzuki, N., 2001. Antioxidative activities of some commercially honeys, royal jelly, and propolis. Food Chem. 75, 237-240. 996 Nagai, T., Inoue, R., 2004. Preparation and the functional properties of water and alkaline extract of royal jelly. Food Chem. 84, 181-186. MICROGRAFII ASUPRA PRODUSELOR APICOLE Andrițoiu Călin Vasile 237 al. (2006997) au confirmat proprietățile antioxidante ale extractului apos și alcalin de LM și hidrolizatele enzimatice de LM. Folosindu-se drojdie ca model de organism și
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